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Overview
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FADD produced in E. Coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-208 a.a.) and having a molecular mass of 27.4 kDa. FADD is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.
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Overview